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Related Experiment Videos

Structure of the iron complex in methemerythrin.

R E Stenkamp, L C Sieker, L H Jensen

    Proceedings of the National Academy of Sciences of the United States of America
    |February 1, 1976
    PubMed
    Summary

    Researchers determined the iron atom coordination in methemerythrin from Themiste dyscritum using electron density maps. The structure reveals two trigonal antiprisms per subunit, with protein side chains and a water molecule coordinating the iron atoms.

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    Area of Science:

    • Structural Biology
    • Biochemistry
    • Protein Crystallography

    Background:

    • Methemerythrin is an iron-containing protein involved in oxygen transport.
    • Understanding the coordination environment of iron atoms is crucial for elucidating protein function.

    Purpose of the Study:

    • To determine the coordination geometry of iron atoms in methemerythrin from Themiste dyscritum.
    • To compare the structural findings with known hemerythrin sequences.

    Main Methods:

    • X-ray crystallography
    • Electron density map analysis at 2.8 A resolution
    • Comparison with amino acid sequence data.

    Main Results:

    • The iron atoms are coordinated by two trigonal antiprisms sharing a common face.

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  • Eight of the nine coordination positions are occupied by protein side chains (five histidine, one tyrosine) and two nonaromatic ligands.
  • The ninth position is likely occupied by a water molecule, forming bridges between iron atoms.

    • Conclusions:

    • The deduced structure provides insights into the active site of methemerythrin.
    • The coordination pattern suggests a functional role in iron-mediated biological processes.